3.3.4.1-3.3.4.2 mass transport in animals & plants Flashcards
(174 cards)
What do RBCs contain?
contains haemoglobin
Describe the structure of haemoglobin
- large water-soluble, globular protein w quarternary structure (made up of more than 1 polypeptide chain)
- 2 pairs of polypeptides chains (alpha and beta)
- each chain has a haem group, which contains an iron ion and gives Haemoglobin its red colour
how many molecules of oxygen can Haemoglobin carry?
- each molecule can carry four oxygen molecules
how and where is oxyhaemoglobin formed?
- in the lungs
- oxygen joins to haemoglobin in red blood cells to form oxyhaemoglobin
Hb + 4O2 –> HbO8
explain what happens in dissociation of oxyhaemoglobin
- reversible reaction
- when red blood cells reach tissue in body (e.g. muscle cells), oxygen is released from Oxyhaemoglobin and it turns back to haemoglobin
haemoglobin is found in all types of what animal?
vertebrates (e.g. earthworms, some insects, some plants and even in some bacteria)
If haemoglobin has a high/low affinity of oxygen, what does this mean?
high:
- take up (associates) oxygen more easily
- but release (dissociates) it less easily
low:
- take up (associates) oxygen less easily
- release it (dissociates) more easily
what must haemoglobin be able to do to make it efficient for transporting oxygen?
- readily associate w/ oxygen at surface where gas exchange takes place
- readily dissociate from oxygen at tissues requiring it
what is haemoblogin able to do under different conditions?
- change its affininity for oxygen under different conditions
describe the affintiy of haemoglobin for oxygen near gas exchange surfaces in terms of: oxygen concentration, carbon dioxide concentration, affinity of haemoglobin for oxygen and the result
oxygen conc: high
CO2 conc: low
affintiy of haemolglobin for O2: high
result: oxygen is associated
describe the affintiy of haemoglobin for oxygen near respiring tissues in terms of: oxygen concentration, carbon dioxide concentration, affinity of haemoglobin for oxygen and the result
oxygen conc: low
CO2 conc: high
affintiy of haemolglobin for O2: low
result: oxygen is dissociated
explain how DNA leads to different haemoglobin molecules having different affinities for oxygen
- affinity of oxygen to haemoglobin depends on haemoglobin structure
- different base sequences in DNA - different AA sequences - different tertiary/ quaternary structure and shape
- so different affinities for oxygen
what is the oxygen dissocation curve?
graph of the relationship between the saturation of haemoglobin with oxygen (%) and the partial pressure of oxygen (kPa)
name three factors affecting oxygen-haemoglobin binding
1 partial pressure of oxygen
2 partial pressure of carbon dioxide
3 saturation of haemoglobin
draw out and explain in detail the oxygen dissociation curve
- initially graph is shallow bc shape of haemoglobin makes it hard for first oxygen molecule to bind to one of the sites on its 4 polypeptide subunits bc they’re closely united (so in low O2 conc, little O2 binds to haemoglobin)
- once first O2 binded it changes the quarternary structure of haemoglobin, causing it to change shape. Makes it easier for other subunits to bind to an O2 molecule (more binding sites revealed!)
- therefore takes a smaller increase in partial pressure of oxygen to bind the 2nd oxygen molceule than the first (this is positive cooperativity bc binding of first makes second easier and so on).
- finally gradient begins to flatten out b/c likelihood of fourth oxygen finding a binding site is low (due to low probability)
what does a further left and further right oxygen dissociation curve indicate?
further left = greater affinity of haemoglobin for oxygen (loads oxygen readily but unloads it less easily)
further right = lower affinity of haemoglobin for oxygen (loads oxygen less readily but unloads it more easily)
explain the affinity of fetal haemoglobin
- fetal haemoglobin has higher affinity for oxygen than adult haemoglobin (curve further left).
- bc it must obtain oxygen from mother’s bloodstream as it doesn’t ventiate (by time oxygen reaches placenta, oxygen saturation in blood has decreased so ppO2 is low)
- this means fetal haemoglobin can bind to oxygen at lower partial pressure so foetus can survive low partial pressure
how does partial pressure of carbon dioxide affect oxygen-haemoglobin?
- as partial pressure of carbon dioxide increases, the conditions become acidic causing haemoglobin to change shape (this is bc CO2 reacts w/ water to form carbonic acid which lowers blood pH), affinity of haemoglobin for oxygen decreases, so oxygen released from haemoglobin
- known as bohr effect
what affect does a greater carbon dioxide concentration have on haemoglobin?
greater carbon dioxide concentration, the more readily the haemoglobin releases its oxygen (the bohr effect)
explain why oxygen binds to haemoglobin at a gas-exchange surface (e.g. THE LUNGS) and affect on oxygen dissociation curve?
- high pO2
- low carbon dioxide concentration in lungs
- therefore affinity of haemoglobin of oxygen increased (positive cooperativity (after first oxygen molecule binds, binding of subsequent molecules is easier)
- reduced CO2 conc has shifted oxygen dissociation curve to the left
why is carbon dioxide concentration low at a gas exchange surface?
because CO2 diffuses across exchange surface and is excreted from organism
explain why oxygen is released from haemoglobin in respiring tisssues (e.g. MUSCLES) and affect on oxygen dissociation curve?
- low pO2
- high carbon dioxide concentration
- CO2 dissolves in blood to form carbonic acid which makes blood acidic
- therefore affinity of haemoglobin of oxygen is reduced, this means oxygen is readily unloaded from haemoglobin into muscle cells
- increased CO2 conc has shifted oxygen dissociation curve to the right
describe the process of how the loading, transport and unloading of oxygen maintains sufficient oxygen for respiring tissues
- at gas-exchange surface, CO2 constantly being removed
- pH slightly raised due to low conc of CO2
- higher pH changes shape of haemoglobin and it loads oxygen more readily
- shape also increases affinity of haemoglobin for oxygen, so its not released while being transported in blood to tissues
- in tissues, CO2 produced by respiring cells
- CO2 is acidic in solution, so pH of blood within tissue lowered, lower pH changes shape of haemoglobin into one w/ a lower affinity for oxygen
- hameoglobin releases its oxygen into respiring tissues
(the more active a tissue, the more oxygen is unloaded)
describe how a higher rate of respiration leads to more oxygen available for respiration
higher rate of respiration - the more carbon dioxide the tissue produce - the lower the pH - greater the haemoglobin shape change - the more readily oxygen is unloaded - the more oxygen is available for respiration